PFKA_CHLAD
ID PFKA_CHLAD Reviewed; 356 AA.
AC B8GAA4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01976};
DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_01976};
DE Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01976};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_01976};
DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_01976};
GN Name=pfkA {ECO:0000255|HAMAP-Rule:MF_01976}; OrderedLocusNames=Cagg_3643;
OS Chloroflexus aggregans (strain MD-66 / DSM 9485).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=326427;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-66 / DSM 9485;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroflexus aggregans DSM 9485.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC fructose 1,6-bisphosphate by ATP, the first committing step of
CC glycolysis. {ECO:0000255|HAMAP-Rule:MF_01976}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01976};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01976};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000255|HAMAP-Rule:MF_01976}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_01976}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01976}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC Mixed-substrate PFK group III subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01976}.
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DR EMBL; CP001337; ACL26479.1; -; Genomic_DNA.
DR RefSeq; WP_015942324.1; NC_011831.1.
DR AlphaFoldDB; B8GAA4; -.
DR SMR; B8GAA4; -.
DR STRING; 326427.Cagg_3643; -.
DR EnsemblBacteria; ACL26479; ACL26479; Cagg_3643.
DR KEGG; cag:Cagg_3643; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_0_0_0; -.
DR OMA; TNRDNPF; -.
DR OrthoDB; 1421302at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000002508; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.460; -; 1.
DR HAMAP; MF_01976; Phosphofructokinase_III; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR012003; ATP_PFK_prok-type.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR012829; Phosphofructokinase_III.
DR InterPro; IPR035966; PKF_sf.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
DR TIGRFAMs; TIGR02483; PFK_mixed; 1.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..356
FT /note="ATP-dependent 6-phosphofructokinase"
FT /id="PRO_1000192367"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 78..79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 115..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 138..140
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 175
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 182..184
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 235
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 272
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 278..281
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT SITE 117
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
SQ SEQUENCE 356 AA; 37734 MW; 66436D7A5E6F4579 CRC64;
MASKKQRIGV LTSGGDAPGL NAVIRAVVKS ASSLGWEVIG IHDGFEGLLG TKSYRVLTNA
DVQGLLPRGG TILRTTNKGH FGPRRSDELS EADPYVRAVK AIEEMGLRAL ITIGGEGTQR
IALELHKLGA PVIGVPKTID NDLAGTDRTF GFDTALQVAT DAIDRLHTTA ASHNRVMVLE
VMGRHTGWIA LHAGLAGGAD VILIPEIPFT IERVAEKVHA RDAQGSAFSI IVVAEGARPR
GGSEMYIAEG RLGGIGHWVG EQLERLTGKD VRVVVLGHLQ RGGSPSPYDR LLSTRYGAAA
VQAAARGIYG EMVALRGQDI VTVPLAEACG YLNRVRPHSD LVLCARSLGI VFGDEL
